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Erythropoietin receptor activation by a ligand-induced conformation change

Academic Article
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Overview

authors

  • Remy, I.
  • Wilson, Ian
  • Michnick, S. W.

publication date

  • February 1999

journal

  • Science  Journal

abstract

  • Erythropoietin and other cytokine receptors are thought to be activated through hormone-induced dimerization and autophosphorylation of JAK kinases associated with the receptor intracellular domains. An in vivo protein fragment complementation assay was used to obtain evidence for an alternative mechanism in which unliganded erythropoietin receptor dimers exist in a conformation that prevents activation of JAK2 but then undergo a ligand-induced conformation change that allows JAK2 to be activated. These results are consistent with crystallographic evidence of distinct dimeric configurations for unliganded and ligand-bound forms of the erythropoietin receptor.

subject areas

  • Animals
  • CHO Cells
  • COS Cells
  • Cricetinae
  • Dimerization
  • Erythropoietin
  • Flow Cytometry
  • Fluoresceins
  • Janus Kinase 2
  • Ligands
  • Methotrexate
  • Microscopy, Fluorescence
  • Peptides, Cyclic
  • Protein Conformation
  • Protein-Tyrosine Kinases
  • Proto-Oncogene Proteins
  • Receptors, Erythropoietin
  • Recombinant Fusion Proteins
  • Tetrahydrofolate Dehydrogenase
  • Transfection
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.283.5404.990

PubMed ID

  • 9974393
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Additional Document Info

start page

  • 990

end page

  • 993

volume

  • 283

issue

  • 5404

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